The X‐ray crystal structure of β‐ketoacyl [acyl carrier protein] synthase I

FEBS Letters

Siggaard-Andersen, Mads²  Larsen, Sine¹  Lindquist, Ylva¹  Kadziola, Anders¹  Olsen, Johan Gotthardt¹  von Wettstein-Knowles, Penny² 

[1] Centre for Crystallographic Studies, University of Copenhagen, Universitetsparken 5, DK-2100 Copenhagen, Denmark;Department of Genetics, Institute of Molecular Biology, University of Copenhagen, Øster Farimagsgade 2A, DK-1353 Copenhagen, Denmark

关键词: Condensing enzyme;    Protein structure;    Fatty acid synthesis;    Escherichia coli;    KAS;    β-ketoacyl [acyl carrier protein] synthase;    FAS;    fatty acid synthase;    ACP;    acyl carrier protein;    NCS;    non-crystallographic symmetry;    PKS;    polyketide synthase;   

DOI  :  10.1016/S0014-5793(99)01303-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The crystal structure of the fatty acid elongating enzyme β-ketoacyl [acyl carrier protein] synthase I (KAS I) from Escherichia coli has been determined to 2.3 Å resolution by molecular replacement using the recently solved crystal structure of KAS II as a search model. The crystal contains two independent dimers in the asymmetric unit. KAS I assumes the thiolase αβαβα fold. Electrostatic potential distribution reveals an acyl carrier protein docking site and a presumed substrate binding pocket was detected extending the active site. Both subunits contribute to each substrate binding site in the dimer.

【 授权许可】

Unknown